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Sci Rep. 2014 Mar 31;4:4524. doi: 10.1038/srep04524.

PSEA: Kinase-specific prediction and analysis of human phosphorylation substrates.

Author information

1
Department of Chemistry, Nanchang University, Nanchang, 330031, China.
2
1] Department of Chemistry, Nanchang University, Nanchang, 330031, China [2] Department of Chemical Engineering, Pingxiang College, Pingxiang, 337055, China.
3
1] Department of Chemistry, Nanchang University, Nanchang, 330031, China [2] Department of Mathematics, Nanchang University, Nanchang, 330031, China.

Abstract

Protein phosphorylation catalysed by kinases plays crucial regulatory roles in intracellular signal transduction. With the increasing number of kinase-specific phosphorylation sites and disease-related phosphorylation substrates that have been identified, the desire to explore the regulatory relationship between protein kinases and disease-related phosphorylation substrates is motivated. In this work, we analysed the kinases' characteristic of all disease-related phosphorylation substrates by using our developed Phosphorylation Set Enrichment Analysis (PSEA) method. We evaluated the efficiency of our method with independent test and concluded that our approach is reliable for identifying kinases responsible for phosphorylated substrates. In addition, we found that Mitogen-activated protein kinase (MAPK) and Glycogen synthase kinase (GSK) families are more associated with abnormal phosphorylation. It can be anticipated that our method might be helpful to identify the mechanism of phosphorylation and the relationship between kinase and phosphorylation related diseases. A user-friendly web interface is now freely available at http://bioinfo.ncu.edu.cn/PKPred_Home.aspx.

PMID:
24681538
PMCID:
PMC3970127
DOI:
10.1038/srep04524
[Indexed for MEDLINE]
Free PMC Article
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